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6CQD

Crystal structure of HPK1 in complex with ATP analogue (AMPPNP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue ANP A 301
ChainResidue
ALEU23
AALA141
AASN142
ALEU144
AASP155
AMG302
AMG303
AHOH402
AHOH405
AHOH418
AHOH445
AGLY26
AHOH480
AHOH498
AVAL31
AALA44
ALYS46
AMET91
AGLU92
ACYS94
AASP101

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AASN142
AASP155
AANP301
AHOH402
AHOH445

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 303
ChainResidue
AASP155
AANP301
AHOH405

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 301
ChainResidue
BASN142
BASP155
BANP302

site_idAC5
Number of Residues15
Detailsbinding site for residue ANP B 302
ChainResidue
BLEU23
BGLY25
BGLY26
BVAL31
BALA44
BLYS46
BMET91
BGLU92
BCYS94
BASP101
BALA141
BASN142
BLEU144
BASP155
BMG301

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGTYGEVFkArdkvsgdl..........VALK
ChainResidueDetails
ALEU23-LYS46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP137
BASP137

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU23
BLYS46
ALEU23
ALYS46

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
BGLU165
BTHR175
AGLU165
ATHR175

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24362026
ChainResidueDetails
AGLU171
BGLU171

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PDB entries from 2024-06-12

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